AbstractInaD, a Drosophila photoreceptor scaffolding protein, assembles multiple signal-transducing proteins at the membrane via its five PDZ domains, enhancing speed and efficiency of vision. Extensive conservation of PDZ domains suggests that these motifs have a general role in organizing diverse signaling complexes
<div><p>PDZ domain-mediated interactions have greatly expanded during metazoan evolution, becoming i...
SummaryTo examine the scaffolding properties of PSD-95, we have taken advantage of established ligan...
AbstractIn Drosophila, the store-operated Ca2+ channel, TRP, is required in photoreceptor cells for ...
InaD, a Drosophila photoreceptor scaffolding protein, assembles multiple signal-transducing proteins...
SummaryThe INAD scaffold organizes a multiprotein complex that is essential for proper visual signal...
SummaryINAD is a scaffolding protein that regulates signaling in Drosophila photoreceptors. One of i...
AbstractPDZ domains are thought to act as protein-binding modules mediating the clustering of membra...
PDZ domains are common building blocks of scaffold proteins that enhance specificity and speed in si...
Here, we reveal a novel feature of the dynamic organization of signaling components in Drosophila ph...
The vast majority of PDZ domains are known to bind to a few C-terminal tail residues of target prote...
AbstractPDZ domains can dimerize or bind to the carboxyl termini of unrelated proteins. Crystallogra...
AbstractThe PDZ domain is a protein–protein interacting module that plays an important role in the o...
Scaffold proteins allow specific protein complexes to be assembled in particular regions of the cell...
Phototransduction in Drosophila is the fastest known G-protein coupled signalingcascade to date. Stu...
Drosophila inactivation no afterpotential D (INAD) is a PDZ domain-containing scaffolding protein th...
<div><p>PDZ domain-mediated interactions have greatly expanded during metazoan evolution, becoming i...
SummaryTo examine the scaffolding properties of PSD-95, we have taken advantage of established ligan...
AbstractIn Drosophila, the store-operated Ca2+ channel, TRP, is required in photoreceptor cells for ...
InaD, a Drosophila photoreceptor scaffolding protein, assembles multiple signal-transducing proteins...
SummaryThe INAD scaffold organizes a multiprotein complex that is essential for proper visual signal...
SummaryINAD is a scaffolding protein that regulates signaling in Drosophila photoreceptors. One of i...
AbstractPDZ domains are thought to act as protein-binding modules mediating the clustering of membra...
PDZ domains are common building blocks of scaffold proteins that enhance specificity and speed in si...
Here, we reveal a novel feature of the dynamic organization of signaling components in Drosophila ph...
The vast majority of PDZ domains are known to bind to a few C-terminal tail residues of target prote...
AbstractPDZ domains can dimerize or bind to the carboxyl termini of unrelated proteins. Crystallogra...
AbstractThe PDZ domain is a protein–protein interacting module that plays an important role in the o...
Scaffold proteins allow specific protein complexes to be assembled in particular regions of the cell...
Phototransduction in Drosophila is the fastest known G-protein coupled signalingcascade to date. Stu...
Drosophila inactivation no afterpotential D (INAD) is a PDZ domain-containing scaffolding protein th...
<div><p>PDZ domain-mediated interactions have greatly expanded during metazoan evolution, becoming i...
SummaryTo examine the scaffolding properties of PSD-95, we have taken advantage of established ligan...
AbstractIn Drosophila, the store-operated Ca2+ channel, TRP, is required in photoreceptor cells for ...
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